NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1382268962|ref|WP_108132551|]
View 

MULTISPECIES: GMP synthase [Halomonas]

Protein Classification

type 1 glutamine amidotransferase family protein( domain architecture ID 73)

type 1 glutamine amidotransferase (GATase1) family protein

CATH:  3.40.50.880
PubMed:  10387030
SCOP:  3001405

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GAT_1 super family cl00020
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 1-235 1.80e-70

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


The actual alignment was detected with superfamily member PRK05665:

Pssm-ID: 469582 [Multi-domain]  Cd Length: 240  Bit Score: 215.83  E-value: 1.80e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962   1 MRIGLLQCDDVAPELIDAHGNYPAMFEALLAPAafslGVSLEWQVYRCLDGEIPDDVEAVDAWLTTGSK---FGVNdghA 77
Cdd:PRK05665    3 LRICILETDVLRPELVAQYQGYGRMFEQLFARQ----PIAAEFVVYNVVQGDYPADDEKFDAYLVTGSKadsFGTD---P 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  78 WIARLEDFVRALYRAEKPLVGVCFGHQLIVKALGGEVIKSPKGWGVGLSNNRVGEREPWMTPWQHDLDLLVSHQDQVETL 157
Cdd:PRK05665   76 WIQTLKTYLLKLYERGDKLLGVCFGHQLLALLLGGKAERASQGWGVGIHRYQLAAHAPWMSPAVTELTLLISHQDQVTAL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382268962 158 PEGASTLGGSGFCPHYLIRVGRCFLGVQGHPEFRPDYSRDLMHLRQGLVGEERVRQGQASLAGRIDDGVMAEWILRFM 235
Cdd:PRK05665  156 PEGATVIASSDFCPFAAYHIGDQVLCFQGHPEFVHDYSRALLDLRQEHLGEEVYSKGVASLAHDHQGTTVAEWMMRFV 233
 
Name Accession Description Interval E-value
PRK05665 PRK05665
amidotransferase; Provisional
 1-235 1.80e-70

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 215.83  E-value: 1.80e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962   1 MRIGLLQCDDVAPELIDAHGNYPAMFEALLAPAafslGVSLEWQVYRCLDGEIPDDVEAVDAWLTTGSK---FGVNdghA 77
Cdd:PRK05665    3 LRICILETDVLRPELVAQYQGYGRMFEQLFARQ----PIAAEFVVYNVVQGDYPADDEKFDAYLVTGSKadsFGTD---P 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  78 WIARLEDFVRALYRAEKPLVGVCFGHQLIVKALGGEVIKSPKGWGVGLSNNRVGEREPWMTPWQHDLDLLVSHQDQVETL 157
Cdd:PRK05665   76 WIQTLKTYLLKLYERGDKLLGVCFGHQLLALLLGGKAERASQGWGVGIHRYQLAAHAPWMSPAVTELTLLISHQDQVTAL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382268962 158 PEGASTLGGSGFCPHYLIRVGRCFLGVQGHPEFRPDYSRDLMHLRQGLVGEERVRQGQASLAGRIDDGVMAEWILRFM 235
Cdd:PRK05665  156 PEGATVIASSDFCPFAAYHIGDQVLCFQGHPEFVHDYSRALLDLRQEHLGEEVYSKGVASLAHDHQGTTVAEWMMRFV 233
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-238 1.53e-55

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 177.45  E-value: 1.53e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962   2 RIGLLQCDDvapelidAHGNYPAMFEALLAPAAFslgvslEWQVYRCLDGEI---PDDVEAVDAWLTTGSKFGVNDGHAW 78
Cdd:COG0518     1 KILILDHDP-------FGGQYPGLIARRLREAGI------ELDVLRVYAGEIlpyDPDLEDPDGLILSGGPMSVYDEDPW 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  79 IARLEDFVRALYRAEKPLVGVCFGHQLIVKALGGEVIKSPkGWGVGLSNNRVGEREPWMTPWQHDLDLLVSHQDQVETLP 158
Cdd:COG0518    68 LEDEPALIREAFELGKPVLGICYGAQLLAHALGGKVEPGP-GREIGWAPVELTEADPLFAGLPDEFTVWMSHGDTVTELP 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962 159 EGASTLGGSGFCPHYLIRVGRCFLGVQGHPEFRPDYSRDLMHLRQGLVGEERVRQgQASLAGRIDDGVMAEWILRFMREA 238
Cdd:COG0518   147 EGAEVLASSDNCPNQAFRYGRRVYGVQFHPEVTHTMMEAWLEERADELAAEELLA-EASLHDPELREAGRRLLRNFLREI 225
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 2-189 4.58e-52

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 167.04  E-value: 4.58e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962   2 RIGLLQCDDVAPelidahgnyPAMFEALLAPAAFslgVSLEWQVYRCLDGEIPDDVEAVDAWLTTGSKFGV-NDGHAWIA 80
Cdd:cd01741     1 RILILQHDTPEG---------PGLFEDLLREAGA---ETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVdEDDYPWLK 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  81 RLEDFVRALYRAEKPLVGVCFGHQLIVKALGGEVIKSPKGWGVG---LSNNRVGEREPWMTPWQHDLDLLVSHQDQVETL 157
Cdd:cd01741    69 KLKELIRQALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGwfpVTLTEAGKADPLFAGLPDEFPVFHWHGDTVVEL 148

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1382268962 158 PEGASTLGGSGFCPHYLIRVGRCFLGVQGHPE 189
Cdd:cd01741   149 PPGAVLLASSEACPNQAFRYGDRALGLQFHPE 180
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 88-204 4.47e-16

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 73.89  E-value: 4.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  88 ALYRAEKPLVGVCFGHQLIVKALGGEVIKSPKGwGVGLSNNRVGEREPWMTPWQHDLDLLVSHQDQVETLPEGASTLGGS 167
Cdd:TIGR00888  65 KIFELGVPVLGICYGMQLMAKQLGGEVGRAEKR-EYGKAELEILDEDDLFRGLPDESTVWMSHGDKVKELPEGFKVLATS 143

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1382268962 168 GFCPHYLIRV-GRCFLGVQGHPEfrpdysrdLMHLRQG 204
Cdd:TIGR00888 144 DNCPVAAMAHeEKPIYGVQFHPE--------VTHTEYG 173
GATase pfam00117
Glutamine amidotransferase class-I;
84-192 1.69e-09

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 55.71  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  84 DFVRALYRAEKPLVGVCFGHQLIVKALGGEVIKSPKGwGVGLSNNRVGEREPWMtpWQHDLDLLV---SHQDQV--ETLP 158
Cdd:pfam00117  61 EAIREARELKIPILGICLGHQLLALAFGGKVVKAKKF-GHHGKNSPVGDDGCGL--FYGLPNVFIvrrYHSYAVdpDTLP 137

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1382268962 159 EGASTLGGS--GFCPHYLIRVGRCFLGVQGHPEFRP 192
Cdd:pfam00117 138 DGLEVTATSenDGTIMGIRHKKLPIFGVQFHPESIL 173
 
Name Accession Description Interval E-value
PRK05665 PRK05665
amidotransferase; Provisional
 1-235 1.80e-70

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 215.83  E-value: 1.80e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962   1 MRIGLLQCDDVAPELIDAHGNYPAMFEALLAPAafslGVSLEWQVYRCLDGEIPDDVEAVDAWLTTGSK---FGVNdghA 77
Cdd:PRK05665    3 LRICILETDVLRPELVAQYQGYGRMFEQLFARQ----PIAAEFVVYNVVQGDYPADDEKFDAYLVTGSKadsFGTD---P 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  78 WIARLEDFVRALYRAEKPLVGVCFGHQLIVKALGGEVIKSPKGWGVGLSNNRVGEREPWMTPWQHDLDLLVSHQDQVETL 157
Cdd:PRK05665   76 WIQTLKTYLLKLYERGDKLLGVCFGHQLLALLLGGKAERASQGWGVGIHRYQLAAHAPWMSPAVTELTLLISHQDQVTAL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1382268962 158 PEGASTLGGSGFCPHYLIRVGRCFLGVQGHPEFRPDYSRDLMHLRQGLVGEERVRQGQASLAGRIDDGVMAEWILRFM 235
Cdd:PRK05665  156 PEGATVIASSDFCPFAAYHIGDQVLCFQGHPEFVHDYSRALLDLRQEHLGEEVYSKGVASLAHDHQGTTVAEWMMRFV 233
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-238 1.53e-55

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 177.45  E-value: 1.53e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962   2 RIGLLQCDDvapelidAHGNYPAMFEALLAPAAFslgvslEWQVYRCLDGEI---PDDVEAVDAWLTTGSKFGVNDGHAW 78
Cdd:COG0518     1 KILILDHDP-------FGGQYPGLIARRLREAGI------ELDVLRVYAGEIlpyDPDLEDPDGLILSGGPMSVYDEDPW 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  79 IARLEDFVRALYRAEKPLVGVCFGHQLIVKALGGEVIKSPkGWGVGLSNNRVGEREPWMTPWQHDLDLLVSHQDQVETLP 158
Cdd:COG0518    68 LEDEPALIREAFELGKPVLGICYGAQLLAHALGGKVEPGP-GREIGWAPVELTEADPLFAGLPDEFTVWMSHGDTVTELP 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962 159 EGASTLGGSGFCPHYLIRVGRCFLGVQGHPEFRPDYSRDLMHLRQGLVGEERVRQgQASLAGRIDDGVMAEWILRFMREA 238
Cdd:COG0518   147 EGAEVLASSDNCPNQAFRYGRRVYGVQFHPEVTHTMMEAWLEERADELAAEELLA-EASLHDPELREAGRRLLRNFLREI 225
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 2-189 4.58e-52

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 167.04  E-value: 4.58e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962   2 RIGLLQCDDVAPelidahgnyPAMFEALLAPAAFslgVSLEWQVYRCLDGEIPDDVEAVDAWLTTGSKFGV-NDGHAWIA 80
Cdd:cd01741     1 RILILQHDTPEG---------PGLFEDLLREAGA---ETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVdEDDYPWLK 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  81 RLEDFVRALYRAEKPLVGVCFGHQLIVKALGGEVIKSPKGWGVG---LSNNRVGEREPWMTPWQHDLDLLVSHQDQVETL 157
Cdd:cd01741    69 KLKELIRQALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGwfpVTLTEAGKADPLFAGLPDEFPVFHWHGDTVVEL 148

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1382268962 158 PEGASTLGGSGFCPHYLIRVGRCFLGVQGHPE 189
Cdd:cd01741   149 PPGAVLLASSEACPNQAFRYGDRALGLQFHPE 180
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 5-240 4.73e-34

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 122.38  E-value: 4.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962   5 LLQCDDVAPELIDAHGNYPAMFEALLAPAafslgvSLEWQVYRCLDGEIPDDVEAVDAWLTTGSKFGVNDGHAWIARLED 84
Cdd:PRK09065    6 IIQTGTPPPSIRARYGDFPHWIRVALGLA------EQPVVVVRVFAGEPLPAPDDFAGVIITGSWAMVTDRLDWSERTAD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  85 FVRALYRAEKPLVGVCFGHQLIVKALGGEVIKSPKGWGVGLSNNRvgerepwMTPWQHDLDLL----------VSHQDQV 154
Cdd:PRK09065   80 WLRQAAAAGMPLLGICYGHQLLAHALGGEVGYNPAGRESGTVTVE-------LHPAAADDPLFaglpaqfpahLTHLQSV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962 155 ETLPEGASTLGGSGFCPHYLIRVGRCFLGVQGHPEFRPDYSRDlmHLRQGLVGEERVRQGQASLAGRIDDGVMAEWIL-R 233
Cdd:PRK09065  153 LRLPPGAVVLARSAQDPHQAFRYGPHAWGVQFHPEFTAHIMRA--YLRARADCLRREGLDARTLLREVSEAPWARKLLrR 230


                  ....*..
gi 1382268962 234 FMREAMA 240
Cdd:PRK09065  231 FVRLARR 237
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 85-189 2.05e-16

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 74.49  E-value: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  85 FVRALYRAEKPLVGVCFGHQLIVKALGGEVIKSPKGwGVGLSNNRVGEREPWMTPWQHDLDLLVSHQDQVETLPEGASTL 164
Cdd:cd01742    62 VDPEIFELGVPVLGICYGMQLIAKALGGKVERGDKR-EYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVKLPEGFKVI 140

                          90       100
                  ....*....|....*....|....*.
gi 1382268962 165 GGSGFCPHYLIR-VGRCFLGVQGHPE 189
Cdd:cd01742   141 ASSDNCPVAAIAnEEKKIYGVQFHPE 166
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 88-204 4.47e-16

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 73.89  E-value: 4.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  88 ALYRAEKPLVGVCFGHQLIVKALGGEVIKSPKGwGVGLSNNRVGEREPWMTPWQHDLDLLVSHQDQVETLPEGASTLGGS 167
Cdd:TIGR00888  65 KIFELGVPVLGICYGMQLMAKQLGGEVGRAEKR-EYGKAELEILDEDDLFRGLPDESTVWMSHGDKVKELPEGFKVLATS 143

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1382268962 168 GFCPHYLIRV-GRCFLGVQGHPEfrpdysrdLMHLRQG 204
Cdd:TIGR00888 144 DNCPVAAMAHeEKPIYGVQFHPE--------VTHTEYG 173
guaA PRK00074
GMP synthase; Reviewed
 88-189 1.65e-13

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 69.31  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  88 ALYRAEKPLVGVCFGHQLIVKALGGEVIKSPKGwGVGLSNNRVGEREPWMTPWQHDLDLLVSHQDQVETLPEGASTLGGS 167
Cdd:PRK00074   70 EIFELGVPVLGICYGMQLMAHQLGGKVERAGKR-EYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIAST 148

                          90       100
                  ....*....|....*....|...
gi 1382268962 168 GFCPHYLIR-VGRCFLGVQGHPE 189
Cdd:PRK00074  149 ENCPIAAIAnEERKFYGVQFHPE 171
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 74-193 2.65e-12

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 64.20  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  74 DGHAWIARLEDFVRALYRAEKPLVGVCFGHQLIVKALGGEVIKSPK---GWGvGLSNNRVGEREPwMTPWQHDLDLLVSH 150
Cdd:PRK07053   64 ELYPFLAPEIALLRQRLAAGLPTLGICLGAQLIARALGARVYPGGQkeiGWA-PLTLTDAGRASP-LRHLGAGTPVLHWH 141

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1382268962 151 QDQVEtLPEGASTLGGSGFCPHYLIRVGRCFLGVQGHPEFRPD 193
Cdd:PRK07053  142 GDTFD-LPEGATLLASTPACRHQAFAWGNHVLALQFHPEARED 183
GATase pfam00117
Glutamine amidotransferase class-I;
84-192 1.69e-09

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 55.71  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  84 DFVRALYRAEKPLVGVCFGHQLIVKALGGEVIKSPKGwGVGLSNNRVGEREPWMtpWQHDLDLLV---SHQDQV--ETLP 158
Cdd:pfam00117  61 EAIREARELKIPILGICLGHQLLALAFGGKVVKAKKF-GHHGKNSPVGDDGCGL--FYGLPNVFIvrrYHSYAVdpDTLP 137

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1382268962 159 EGASTLGGS--GFCPHYLIRVGRCFLGVQGHPEFRP 192
Cdd:pfam00117 138 DGLEVTATSenDGTIMGIRHKKLPIFGVQFHPESIL 173
PRK00758 PRK00758
GMP synthase subunit A; Validated
 89-189 2.31e-09

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 55.24  E-value: 2.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  89 LYRAEKPLVGVCFGHQLIVKALGGEVIKSPKGwGVGLSNNRVGERE-------PWMTPWQhdldllvSHQDQVETLPEGA 161
Cdd:PRK00758   63 LKELDVPILGICLGHQLIAKAFGGEVGRGEYG-EYALVEVEILDEDdilkglpPEIRVWA-------SHADEVKELPDGF 134

                          90       100
                  ....*....|....*....|....*....
gi 1382268962 162 STLGGSGFCPHYLIR-VGRCFLGVQGHPE 189
Cdd:PRK00758  135 EILARSDICEVEAMKhKEKPIYGVQFHPE 163
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 45-236 1.47e-08

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 53.43  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  45 VYR-CLDGEIPDDVEAVDAWLTTGSKFGVNDGHAWIARLEDFVRALYRAEKPLVGVCFGHQLIVKALGGEVIKSPKGWG- 122
Cdd:PRK06490   37 IRRpRLGDPLPDTLEDHAGAVIFGGPMSANDPDDFIRREIDWISVPLKENKPFLGICLGAQMLARHLGARVAPHPDGRVe 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962 123 VGLSNNRVGEREPWMTPW-QHdldllVSH-QDQVETLPEGASTLGGSGFCPHYLIRVGRCFLGVQGHPEFrpdySRDLMH 200
Cdd:PRK06490  117 IGYYPLRPTEAGRALMHWpEM-----VYHwHREGFDLPAGAELLATGDDFPNQAFRYGDNAWGLQFHPEV----TRAMMH 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1382268962 201 lRQGLVGEERV-----RQGQASLAGR-IDDGVMAEWILRFMR 236
Cdd:PRK06490  188 -RWVVRGAHRLtlpgaQPRRAHLEGRlLHDAALRAWLEAFLD 228
PRK07567 PRK07567
glutamine amidotransferase; Provisional
 47-189 5.12e-08

glutamine amidotransferase; Provisional


Pssm-ID: 181035 [Multi-domain]  Cd Length: 242  Bit Score: 52.25  E-value: 5.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  47 RCLD-GEIPD-DVEAVDAWLTTGSKFGVNDG-----------HAWIARLEDFVRAlyrAEKPLVGVCFGHQLIVKALGGE 113
Cdd:PRK07567   37 IRLDrEPLPDlDLDDYSGVIVGGSPFNVSDPaeskspwqrrvEAELSGLLDEVVA---RDFPFLGACYGVGTLGHHQGGV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962 114 VIKS-PKGWG---VGLSNNrvGEREPWMTPWQHDLDLLVSHQDQVETLPEGASTLGGSGFCPHYLIRVGRCFLGVQGHPE 189
Cdd:PRK07567  114 VDRTyGEPVGavtVSLTDA--GRADPLLAGLPDTFTAFVGHKEAVSALPPGAVLLATSPTCPVQMFRVGENVYATQFHPE 191
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 82-119 2.10e-06

Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 46.57  E-value: 2.10e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1382268962  82 LEDFVRALYRaEKPLVGVCFGHQLIVKALGGEVIKSPK 119
Cdd:COG0512    61 SLEVIRAFAG-KIPILGVCLGHQAIGEAFGGKVVRAPE 97
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 15-107 3.13e-06

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 44.90  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  15 LIDAHGNYPAMFEALLApAAFSLGVslEWQVYRCLDGEIP--DDVEAVDAWLTTGSkFGVNDGHAWIARLEDFVRALYRA 92
Cdd:cd01653     3 VLLFPGFEELELASPLD-ALREAGA--EVDVVSPDGGPVEsdVDLDDYDGLILPGG-PGTPDDLARDEALLALLREAAAA 78

                          90
                  ....*....|....*
gi 1382268962  93 EKPLVGVCFGHQLIV 107
Cdd:cd01653    79 GKPILGICLGAQLLV 93
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 82-119 5.38e-06

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 45.51  E-value: 5.38e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1382268962  82 LEDFVRALYRaEKPLVGVCFGHQLIVKALGGEVIKSPK 119
Cdd:PRK05670   62 SLELIREFAG-KVPILGVCLGHQAIGEAFGGKVVRAKE 98
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 86-119 6.00e-06

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 45.22  E-value: 6.00e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1382268962  86 VRALYRAEKPLVGVCFGHQLIVKALGGEVIKSPK 119
Cdd:cd01743    64 IIRALAGKVPILGVCLGHQAIAEAFGGKVVRAPE 97
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
86-116 7.63e-06

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 46.22  E-value: 7.63e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1382268962  86 VRALYRAEKPLVGVCFGHQLIVKALGGEVIK 116
Cdd:PRK12564  241 IRELLEKKIPIFGICLGHQLLALALGAKTYK 271
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 86-116 9.10e-06

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 45.78  E-value: 9.10e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1382268962  86 VRALYRAEKPLVGVCFGHQLIVKALGGEVIK 116
Cdd:COG0505   240 IRELLGKGIPIFGICLGHQLLALALGAKTYK 270
PLN02347 PLN02347
GMP synthetase
 95-189 2.05e-05

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 45.06  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  95 PLVGVCFGHQLIVKALGGEVIKSPKG-WG-----VGLSNNRVGEREP------WMtpwqhdldllvSHQDQVETLPEGAS 162
Cdd:PLN02347   88 PVLGICYGMQLIVQKLGGEVKPGEKQeYGrmeirVVCGSQLFGDLPSgetqtvWM-----------SHGDEAVKLPEGFE 156

                          90       100
                  ....*....|....*....|....*...
gi 1382268962 163 TLGGSGFCPHYLIR-VGRCFLGVQGHPE 189
Cdd:PLN02347  157 VVAKSVQGAVVAIEnRERRIYGLQYHPE 184
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 15-106 2.15e-05

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 42.19  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  15 LIDAHGNYPAMFEALLApAAFSLGVslEWQVYRCLDGEIPDDVEA--VDAWLTTGSkFGVNDGHAWIARLEDFVRALYRA 92
Cdd:cd03128     3 VLLFGGSEELELASPLD-ALREAGA--EVDVVSPDGGPVESDVDLddYDGLILPGG-PGTPDDLAWDEALLALLREAAAA 78

                          90
                  ....*....|....
gi 1382268962  93 EKPLVGVCFGHQLI 106
Cdd:cd03128    79 GKPVLGICLGAQLL 92
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 84-116 3.49e-04

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 40.17  E-value: 3.49e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1382268962  84 DFVRALYRAEKPLVGVCFGHQLIVKALGGEVIK 116
Cdd:cd01744    60 KTVRKLLGKKIPIFGICLGHQLLALALGAKTYK 92
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 92-193 4.58e-04

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 40.34  E-value: 4.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  92 AEKPLVGVCFGHQLIVKALGGEVIKSPkgwgvglsnnrvgEREPWMTPWQ------HD-------LDLLVSH-QDQVETL 157
Cdd:PRK08250   83 AGKAVIGVCLGAQLIGEALGAKYEHSP-------------EKEIGYFPITlteaglKDpllshfgSTLTVGHwHNDMPGL 149

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1382268962 158 PEGASTLGGSGFCPHYLIRVGRCFLGVQGHPEFRPD 193
Cdd:PRK08250  150 TDQAKVLATSEGCPRQIVQYSNLVYGFQCHMEFTVE 185
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
84-118 5.07e-04

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 40.03  E-value: 5.07e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1382268962  84 DFVRALYRAEKPLVGVCFGHQLIVKALGGEVIKSP 118
Cdd:PRK07765   67 DMVRACAAAGTPLLGVCLGHQAIGVAFGATVDRAP 101
PLN02335 PLN02335
anthranilate synthase
 95-120 5.26e-04

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 40.17  E-value: 5.26e-04
                          10        20
                  ....*....|....*....|....*.
gi 1382268962  95 PLVGVCFGHQLIVKALGGEVIKSPKG 120
Cdd:PLN02335   93 PLFGVCMGLQCIGEAFGGKIVRSPFG 118
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
95-119 1.39e-03

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 38.63  E-value: 1.39e-03
                          10        20
                  ....*....|....*....|....*
gi 1382268962  95 PLVGVCFGHQLIVKALGGEVIKSPK 119
Cdd:PRK07649   74 PIFGVCLGHQSIAQVFGGEVVRAER 98
trpG CHL00101
anthranilate synthase component 2
 95-119 2.06e-03

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 38.17  E-value: 2.06e-03
                          10        20
                  ....*....|....*....|....*
gi 1382268962  95 PLVGVCFGHQLIVKALGGEVIKSPK 119
Cdd:CHL00101   74 PILGVCLGHQSIGYLFGGKIIKAPK 98
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
73-119 4.15e-03

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 37.16  E-value: 4.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1382268962  73 NDGHAWIARLEDFVRALyraekPLVGVCFGHQLIVKALGGEVIKSPK 119
Cdd:PRK08857   57 NEAGISLQAIEHFAGKL-----PILGVCLGHQAIAQVFGGQVVRARQ 98
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 95-192 7.23e-03

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 37.18  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382268962  95 PLVGVCFGHQLIVKALGGEVIKSPKGWGVG------LSNNRVgerepWMTPWQHDLDLLvshqdqvetlpegASTLGGSG 168
Cdd:PRK12838  239 PILGICLGHQLIALALGADTEKLPFGHRGAnhpvidLTTGRV-----WMTSQNHGYVVD-------------EDSLDGTP 300

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1382268962 169 FCPHY----------LIRVGRCFLGVQGHPEFRP 192
Cdd:PRK12838  301 LSVRFfnvndgsiegLRHKKKPVLSVQFHPEAHP 334
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH